IndraLab

Statements

OTUD1 binds STAT3. 20 / 20
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"Further investigation revealed that OTUD1 directly interacts with STAT3, a pivotal transcription factor in the JAK-STAT signaling cascade."
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"This cascade culminates in the OTUD1-STAT3 axis-driven transcriptional repression of PD-L1 in RCC cells."
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"The co-IP and glutathione S-transferase (GST) pull-down assays indicated that STAT3 interacts with OTUD1 endogenously and exogenously in ccRCC cells (Fig.  xref D, E)."
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"This study further elucidated that OTUD1 bound to the SH2 domain of STAT3 through its cysteine site at position 320, thereby exerting the effect of deubiquitination (Ref. xref )."
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"In the above experiments, we found that OTUD1 interacts with STAT3, suggesting that OTUD1 may regulate PD-L1 through STAT3."
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"Subsequently, through mass spectrometry analysis and immunoprecipitation experiments, we demonstrate that OTUD1 interacts with STAT3 and deubiquitinates, inhibits its nuclear translocation and activity, and ultimately inhibits immune response of ccRCC by downregulating PD-L1."
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"Here, we found that OTUD1 can bind to STAT3 and mediate its ubiquitination modification, inhibiting the activity of STAT3 and its entry into the nucleus, ultimately participating in the immune regulation of renal cell carcinoma tumors."
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"OTUD1 interacts with STAT3 in ccRCC cells lines."
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"These results indicate that STAT3 binds to OTUD1 directly via STAT3 SH2 domain."
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"We tested the idea that OTUD1 binding to STAT3 may disrupt STAT3-KPNA3 association, which possibly reduces nuclear translocation."
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"After identifying STAT3-OTUD1 interaction site, we mutated active sites on OTUD1 (cysteine at position 320 to serine) (Figure xref E)."
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"Mechanistically, we showed that OTUD1 binds to STAT3 and causes deubiquitination of STAT3."
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"Overall, we demonstrate that OTUD1 interacts with STAT3 and deubiquitinates, inhibits its nuclear translocation and activity, and ultimately inhibits immune evasion of ccRCC by downregulating PD-L1."
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"To confirm this potential interaction between OTUD1 and STAT3, we transfected NVRMs and HEK-293T cells with Flag-tagged OTUD1 and showed that STAT3 interacts with OTUD1 following co-IP assay (Figure 5C-D)."
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"Mechanistically, we showed that OTUD1 binds to STAT3 and causes deubiquitination of STAT3."
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"Our detailed mechanistic studies showed that OTUD1 interacts with signal transducer and activator of transcription 3 (STAT3) and leads to deubiquitination and increased phosphorylation of STAT3."
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"OTUD1 interacts directly with STAT3 and promotes STAT3 activation."
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"Representative MS spectra of STAT3 is shown in Figure xref B. To confirm this potential interaction between OTUD1 and STAT3, we transfected NVRMs and HEK-293T cells with Flag-tagged OTUD1 and showed that STAT3 interacts with OTUD1 following co-IP assay (Figure xref C-D)."
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"We tested the idea that OTUD1 binding to STAT3 may disrupt STAT3-KPNA3 association, which possibly reduces nuclear translocation."
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"These in vitro studies show that OTUD1 interacts with STAT3 and regulates Tyr-705 phosphorylation and nuclear translocation to module expression of cardiac remodeling genes."
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